Structural highlights
Function
ERYC3_SACEN Catalyzes the conversion of alpha-L-mycarosylerythronolide B into erythromycin D in the erythromycin biosynthesis pathway.[1]
Publication Abstract from PubMed
In the biosynthesis of the clinically important antibiotic erythromycin D, the glycosyltransferase (GT) EryCIII, in concert with its partner EryCII, attaches a nucleotide-activated sugar to the macrolide scaffold with high specificity. To understand the role of EryCII, we have determined the crystal structure of the EryCIII.EryCII complex at 3.1 A resolution. The structure reveals a heterotetramer with a distinctive, elongated quaternary organization. The EryCIII subunits form an extensive self-complementary dimer interface at the center of the complex, and the EryCII subunits lie on the periphery. EryCII binds in the vicinity of the putative macrolide binding site of EryCIII but does not make direct interactions with this site. Our biophysical and enzymatic data support a model in which EryCII stabilizes EryCIII and also functions as an allosteric activator of the GT.
Structure of the Glycosyltransferase EryCIII in Complex with its Activating P450 Homologue EryCII.,Moncrieffe MC, Fernandez MJ, Spiteller D, Matsumura H, Gay NJ, Luisi BF, Leadlay PF J Mol Biol. 2012 Jan 6;415(1):92-101. Epub 2011 Oct 25. PMID:22056329[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee HY, Chung HS, Hang C, Khosla C, Walsh CT, Kahne D, Walker S. Reconstitution and characterization of a new desosaminyl transferase, EryCIII, from the erythromycin biosynthetic pathway. J Am Chem Soc. 2004 Aug 18;126(32):9924-5. PMID:15303858 doi:http://dx.doi.org/10.1021/ja048836f
- ↑ Moncrieffe MC, Fernandez MJ, Spiteller D, Matsumura H, Gay NJ, Luisi BF, Leadlay PF. Structure of the Glycosyltransferase EryCIII in Complex with its Activating P450 Homologue EryCII. J Mol Biol. 2012 Jan 6;415(1):92-101. Epub 2011 Oct 25. PMID:22056329 doi:10.1016/j.jmb.2011.10.036
